3.5.2.20: isatin hydrolase
This is an abbreviated version!
For detailed information about isatin hydrolase, go to the full flat file.
Reaction
Synonyms
IH-b, isatin amidohydrolase, isatin hydrolase A, isatin hydrolase b, LaIHA, RsIHA
ECTree
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Metals Ions
Metals Ions on EC 3.5.2.20 - isatin hydrolase
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Mn2+
Mn2+
Roseibium aggregatum
highest hydrolytic activity measured in the presence of Mn2+. The highly conserved Mn2+ binding site is located at the bottom of the substrate-binding pocket. The Mn2+ is found in an octahedral complex coordinated by His69, His73, Asp75, and two water molecules. The Mn2+ binding sites includes Gln219
Mn2+
Roseibium aggregatum
structural origin of metal specificity in isatin hydrolase from Labrenzia aggregata is investigated by computer simulations. The peculiar octahedral binding geometry of the Mn2+ ion in the Michaelis complex includes both the isatin substrate and the catalytic water within the first coordination shell of the cation. Calculations show that the same arrangement of the ligands cannot be efficiently achieved in the presence of other small divalent metal cations such as Zn2+ or Cu2+. Bulkier alkaline-earth cations such as Mg2+, which allow octahedral coordination, are not able to activate the catalytic water into the stronger OH- nucleophile required to attack the stable N-aryl-amide moiety of isatin